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THYX_MYCMM
ID   THYX_MYCMM              Reviewed;         250 AA.
AC   B2HKZ0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Flavin-dependent thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_01408};
DE            Short=FDTS {ECO:0000255|HAMAP-Rule:MF_01408};
DE            EC=2.1.1.148 {ECO:0000255|HAMAP-Rule:MF_01408};
DE   AltName: Full=FAD-dependent thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_01408};
DE   AltName: Full=Thymidylate synthase ThyX {ECO:0000255|HAMAP-Rule:MF_01408};
DE            Short=TS {ECO:0000255|HAMAP-Rule:MF_01408};
DE            Short=TSase {ECO:0000255|HAMAP-Rule:MF_01408};
GN   Name=thyX {ECO:0000255|HAMAP-Rule:MF_01408}; OrderedLocusNames=MMAR_1961;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(2008).
CC   -!- FUNCTION: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-
CC       monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while
CC       utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor,
CC       and NADPH and FADH(2) as the reductant. {ECO:0000255|HAMAP-
CC       Rule:MF_01408}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP + H(+) +
CC         NADPH = (6S)-5,6,7,8-tetrahydrofolate + dTMP + NADP(+);
CC         Xref=Rhea:RHEA:29043, ChEBI:CHEBI:15378, ChEBI:CHEBI:15636,
CC         ChEBI:CHEBI:57453, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC         ChEBI:CHEBI:63528, ChEBI:CHEBI:246422; EC=2.1.1.148;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01408};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01408};
CC       Note=Binds 4 FAD per tetramer. Each FAD binding site is formed by three
CC       monomers. {ECO:0000255|HAMAP-Rule:MF_01408};
CC   -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01408}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01408}.
CC   -!- SIMILARITY: Belongs to the thymidylate synthase ThyX family.
CC       {ECO:0000255|HAMAP-Rule:MF_01408}.
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DR   EMBL; CP000854; ACC40411.1; -; Genomic_DNA.
DR   RefSeq; WP_012393751.1; NC_010612.1.
DR   AlphaFoldDB; B2HKZ0; -.
DR   SMR; B2HKZ0; -.
DR   STRING; 216594.MMAR_1961; -.
DR   EnsemblBacteria; ACC40411; ACC40411; MMAR_1961.
DR   GeneID; 64260647; -.
DR   KEGG; mmi:MMAR_1961; -.
DR   eggNOG; COG1351; Bacteria.
DR   HOGENOM; CLU_077585_1_0_11; -.
DR   OMA; AKLGPRC; -.
DR   OrthoDB; 896350at2; -.
DR   UniPathway; UPA00575; -.
DR   Proteomes; UP000001190; Chromosome.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0050797; F:thymidylate synthase (FAD) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1360.170; -; 1.
DR   Gene3D; 3.30.70.3180; -; 1.
DR   HAMAP; MF_01408; ThyX; 1.
DR   InterPro; IPR003669; Thymidylate_synthase_ThyX.
DR   InterPro; IPR036098; Thymidylate_synthase_ThyX_sf.
DR   PANTHER; PTHR34934; PTHR34934; 1.
DR   Pfam; PF02511; Thy1; 1.
DR   SUPFAM; SSF69796; SSF69796; 1.
DR   TIGRFAMs; TIGR02170; thyX; 1.
DR   PROSITE; PS51331; THYX; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Methyltransferase; NADP; Nucleotide biosynthesis;
KW   Reference proteome; Transferase.
FT   CHAIN           1..250
FT                   /note="Flavin-dependent thymidylate synthase"
FT                   /id="PRO_1000184594"
FT   DOMAIN          7..233
FT                   /note="ThyX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00661"
FT   MOTIF           95..105
FT                   /note="ThyX motif"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   ACT_SITE        199
FT                   /note="Involved in ionization of N3 of dUMP, leading to its
FT                   activation"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         92..95
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         95..97
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         103..107
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         103
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         172
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         188..190
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         194
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /ligand_note="ligand shared between neighboring subunits"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
FT   BINDING         199
FT                   /ligand="dUMP"
FT                   /ligand_id="ChEBI:CHEBI:246422"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01408"
SQ   SEQUENCE   250 AA;  27606 MW;  AC43DA49A591A2F9 CRC64;
     MAETAPLRVQ LIAKTEFLAP PDVPWTTDAD GGEALVEFAG RACYQSWSKP NPKTATNAGY
     LRHIIDVGHF AVLEHASVSF YISGISRSCT HELIRHRHFS YSQLSQRYVP EGDSRVVVPP
     GLEDDPELRE ILIAAADASR ATYTELLTKL EARFADQPNA VLRRKQARQA ARAVLPNATE
     TRIVVSGNYR AWRHFIAMRA SEHADVEIRR LAIECLRQLV AVAPAVFADF EVTTLADGSE
     VATSPLATEV
 
 
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